1kuz

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{{Seed}}
 
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[[Image:1kuz.png|left|200px]]
 
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==Solution Structure of the Membrane Proximal Regions of alpha-IIb and beta-3 Integrins==
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The line below this paragraph, containing "STRUCTURE_1kuz", creates the "Structure Box" on the page.
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<StructureSection load='1kuz' size='340' side='right'caption='[[1kuz]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1kuz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KUZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kuz OCA], [https://pdbe.org/1kuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kuz RCSB], [https://www.ebi.ac.uk/pdbsum/1kuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kuz ProSAT]</span></td></tr>
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{{STRUCTURE_1kuz| PDB=1kuz | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[https://omim.org/entry/273800 273800]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref> <ref>PMID:7508443</ref> <ref>PMID:7706461</ref> <ref>PMID:8704171</ref> <ref>PMID:9215749</ref> <ref>PMID:9473221</ref> <ref>PMID:9763559</ref> <ref>PMID:9722314</ref> <ref>PMID:9734640</ref> <ref>PMID:9920835</ref> <ref>PMID:10607701</ref> <ref>PMID:11798398</ref> <ref>PMID:12181054</ref> <ref>PMID:12083483</ref> <ref>PMID:12424194</ref> <ref>PMID:12506038</ref> <ref>PMID:15099289</ref> <ref>PMID:15219201</ref> <ref>PMID:17018384</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN] Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Integrin adhesion receptors constitute a cell-signaling system whereby interactions in the small cytoplasmic domains of the heterodimeric alpha- and beta-subunits provoke major functional alterations in the large extracellular domains. With two-dimensional NMR spectroscopy, we examined two synthetic peptides [alphaIIb((987)MWKVGFFKRNR) and beta3((716)KLLITIHDRKEFAKFEEERARAKWD)] encompassing the membrane-proximal regions of the cytoplasmic domain motifs from the platelet integrin complex alphaIotaIotabbeta3. These membrane-proximal regions contain two conserved motifs, represented by (989)KVGFFKR in the alphaIIb-subunit, and (716)KLLITIHDR in the beta3-subunit. The dimer interaction consists of two adjacent helices with residues V990 and F993 of the alphaIotaIotab-subunit heavily implicated in the dimer interfacial region, as is I719 of beta3. These residues are situated within the conserved motifs of their respective proteins. Further structural analysis of this unique peptide heterodimer suggests that two distinct conformers are present. The major structural difference between the two conformers is a bend in the beta3-peptide between D723 and A728, whereas the helical character in the other regions remains intact. Earlier mutational analysis has shown that a salt bridge between the side chains of alphaIotaIotab(R955) and beta3(D723) is formed. When this ion pair was modeled into both conformers, increased nuclear Overhauser effect violations suggested that the more bent structure was less able to accommodate this interaction. These results provide a molecular level rationalization for previously reported biochemical studies, as well as a basis for an atomic level understanding of the intermolecular interactions that regulate integrin activity.
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===Solution Structure of the Membrane Proximal Regions of alpha-IIb and beta-3 Integrins===
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Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits.,Weljie AM, Hwang PM, Vogel HJ Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5878-83. PMID:11983888<ref>PMID:11983888</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kuz" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11983888}}, adds the Publication Abstract to the page
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*[[Integrin 3D structures|Integrin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11983888 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11983888}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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1KUZ is a [[Protein complex]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUZ OCA].
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[[Category: Large Structures]]
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[[Category: Hwang PM]]
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==Reference==
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[[Category: Vogel HJ]]
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Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits., Weljie AM, Hwang PM, Vogel HJ, Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5878-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11983888 11983888]
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[[Category: Weljie AM]]
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[[Category: Protein complex]]
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[[Category: Hwang, P M.]]
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[[Category: Vogel, H J.]]
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[[Category: Weljie, A M.]]
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[[Category: Coiled-coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:03:16 2008''
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Current revision

Solution Structure of the Membrane Proximal Regions of alpha-IIb and beta-3 Integrins

PDB ID 1kuz

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